Serine-arginine protein kinases and their targets in viral infection and their inhibition.
Alternative splicing
Antiviral
SR proteins
Serine-arginine protein kinases
Virus–host interaction
Journal
Cellular and molecular life sciences : CMLS
ISSN: 1420-9071
Titre abrégé: Cell Mol Life Sci
Pays: Switzerland
ID NLM: 9705402
Informations de publication
Date de publication:
17 May 2023
17 May 2023
Historique:
received:
21
03
2023
accepted:
12
05
2023
revised:
10
05
2023
medline:
19
5
2023
pubmed:
18
5
2023
entrez:
17
5
2023
Statut:
epublish
Résumé
Accumulating evidence has consolidated the interaction between viral infection and host alternative splicing. Serine-arginine (SR) proteins are a class of highly conserved splicing factors critical for the spliceosome maturation, alternative splicing and RNA metabolism. Serine-arginine protein kinases (SRPKs) are important kinases that specifically phosphorylate SR proteins to regulate their distribution and activities in the central pre-mRNA splicing and other cellular processes. In addition to the predominant SR proteins, other cytoplasmic proteins containing a serine-arginine repeat domain, including viral proteins, have been identified as substrates of SRPKs. Viral infection triggers a myriad of cellular events in the host and it is therefore not surprising that viruses explore SRPKs-mediated phosphorylation as an important regulatory node in virus-host interactions. In this review, we briefly summarize the regulation and biological function of SRPKs, highlighting their involvement in the infection process of several viruses, such as viral replication, transcription and capsid assembly. In addition, we review the structure-function relationships of currently available inhibitors of SRPKs and discuss their putative use as antivirals against well-characterized viruses or newly emerging viruses. We also highlight the viral proteins and cellular substrates targeted by SRPKs as potential antiviral therapeutic candidates.
Identifiants
pubmed: 37198350
doi: 10.1007/s00018-023-04808-6
pii: 10.1007/s00018-023-04808-6
pmc: PMC10191411
doi:
Substances chimiques
Protein Kinases
EC 2.7.-
Protein Serine-Threonine Kinases
EC 2.7.11.1
Arginine
94ZLA3W45F
Serine
452VLY9402
Viral Proteins
0
Serine-Arginine Splicing Factors
170974-22-8
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
153Subventions
Organisme : National Natural Science Foundation of China
ID : 82072274
Organisme : the Basic and Applied Basic Research Foundation of Guangdong Province
ID : 2021B1515120088
Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer Nature Switzerland AG.
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